(αMe)Nva: Stereoselective syntheses and preferred conformations of selected model peptides

Journal of Peptide Research

Volumn 56, Issue 5, 2000, Pages 283-297

  Moretto, A ^a   Peggion, C ^a   Formaggio, F ^a   Crisma, M ^a   Toniolo, C ^a   Piazza, C ^b   Kaptein, B ^b   Broxterman, Q B ^b   Ruiz, I ^c   Diaz de Villegas, M D ^c   Galvez, J A ^c   Cativiela, C ^c  

^a UNIVERSITY OF PADOVA   (Italy)

^b DSM RESEARCH   (Netherlands)

^c UNIVERSITY OF ZARAGOZA   (Spain)

Author keywords

aminoisobutyric acid; turn; 310 helix; Asymmetric synthesis; C( ) methyl norvaline; Norvaline; Peptide synthesis; Spectroscopy; X ray diffraction

Indexed keywords

2 AMINO 2 METHYLPENTANOIC ACID; 2 AMINO 2 METHYLPROPIONIC ACID; ALPHA AMINO ACID; UNCLASSIFIED DRUG; 2 METHYLNORVALINE; 2-METHYLNORVALINE; AMINE OXIDE; DRUG DERIVATIVE; OLIGOPEPTIDE; TEMPO; VALINE;

ARTICLE; CHIRALITY; HYDROGENATION; INFRARED SPECTROSCOPY; PEPTIDE SYNTHESIS; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTON NUCLEAR MAGNETIC RESONANCE; STEREOCHEMISTRY; X RAY DIFFRACTION; CHEMICAL STRUCTURE; CHEMISTRY; CRYSTALLIZATION; HYDROGEN BOND; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN SECONDARY STRUCTURE; SOLUTION AND SOLUBILITY; STEREOISOMERISM; SYNTHESIS;

CRYSTALLIZATION; CYCLIC N-OXIDES; HYDROGEN BONDING; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; OLIGOPEPTIDES; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SOLUTIONS; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; STEREOISOMERISM; VALINE; X-RAY DIFFRACTION;

EID: 0033626499     PISSN: 1397002X     EISSN: None     Source Type: Journal    
DOI: 10.1034/j.1399-3011.2000.00768.x     Document Type: Article

References (55)

1. Peptide backbone modifications. A structure-activity analysis of peptides containing amide bond surrogates, conformational constraints, and related backbone replacements
2. Modulations conformationnelles du repliement β en serie peptidique et pseudopeptidique
3. Emerging approaches in the molecular design of receptor-selective peptide ligands: Conformational, topographical and dynamic considerations
4. Structural characteristics of α-helical peptide molecules containing Aib residues
5. Conformationally restricted peptides through short-range cyclizations
6. Structures of polypeptides from α-amino acids disubstituted at the α-carbon
7. Non-standard amino acids in peptide design and protein engineering
8. Structures of peptides from α-amino acids methylated at the α-carbon
9. C(α,α)-Symmetrically disubstituted glycines: Useful building blocks in the design of conformationally restricted peptides
10. Design of peptides, proteins, and peptidomimetics in χ space
11. Peptides that contain unnatural amino acids: Toward artificial proteins
12. 10-helical structure
13. Peptides from chiral C(α,α)-disubstituted glycines. On the helical screw sense of isovaline peptides
14. Preferred solution conformation of peptides rich in the lipophilic, chiral, C(α)-methylated α-amino acid (αMe) Aoc
15. (αMe) Aun: A highly lipophilic, chiral, C(α)-tetrasubstituted α-amino acid. Incorporation into model peptides and preferred conformation
16. Studies on the conformation of Boc-protected (S)-(+)-isovaline homopeptide methyl esters in the solid state and in solution
17. Mag: A C(α)-methylated, side-chain unsaturated α-amino acid. Introduction into model peptides and conformational preference
18. Some derivatives of 1-aminocyclopentanecarboxylic acid and related compounds
19. A new approach to the stereoselective synthesis of conveniently protected α-allyl substituted amino acids; chiral key compounds in the synthesis of constrained peptide isostere constituents
20. A graphics model building and refinement system for macromolecules
21. Stereoselective synthesis of quaternary α-amino acids. Part 1: Acyclic compounds
22. Synthesis of optically pure α-alkylated α-amino acids and a single-step method for enantiomeric excess determination
23. Industrial developments in biocatalysis
24. Enzymatic resolution of α,α-disubstituted α-amino acid esters and amides
25. Quantitative analyses of biochemical kinetic resolutions of enantiomers
26. Ochrobactrum anthropi NCIMB 40231: A new biocatalyst with broad spectrum L-specific amidase activity
27. 1-Hydroxy-7-azabenzotriazole. An efficient peptide coupling reagent
28. Synthesis of (optically active) sulfur-containing trifunctional amino acids by radical addition to (optically active) unsaturated amino acids
29. Conformational analysis of linear peptides: 5. Spectroscopic characterization of β-turns in Aib-containing oligopeptides in chloroform
30. Comparison of the effect of five guest residues on the β-sheet conformation of host (L-Val)(n) oligopeptides
31. The γ-turn, a possible folded conformation of the polypeptide chain. Comparison with the β-turn
32. Intramolecularly hydrogen-bonded peptide conformations
33. Stereochemical criteria for polypeptides and proteins. V. Conformation of a system of three-linked peptide units
34. Turns in peptides and proteins
35. 10-helix
36. Proton magnetic resonance line broadening produced by association with a nitroxide radical in studies of amide and peptide conformation
37. Preferred conformation of the tert-butoxycarbonylamino group in peptides
38. Structural characteristics of the carboxylic ester group
39. Structure and conformation of peptides as determined by X-ray crystallography
40. Peptide chain structure parameters, bond angles and conformational angles from the Cambridge structural database
41. Sensitivity of polypeptide conformation to geometry. Theoretical conformational analysis of oligomers of α-aminoisobutyric acid
42. Geometry and conformation of the α-aminoisobutyric acid residue in simple derivatives and dipeptides. Four new X-ray structural analyses and a statistical analysis from known crystal data
43. Study of hydrogen bonds in amino acids and peptides
44. The geometry of the N-H···O=C hydrogen bond. 3. Hydrogen bond distances and angles
45. Hydrogen bond distances and angles in the structures of amino acids and peptides
46. Preferred conformation of peptides containing α,α-disubstituted α-amino acids
47. Preferred conformation of the carboxyl group
48. Secondary structures in protected homo-oligo-L-norvalines. Comparison with isomeric valines
49. Conformational analysis of protected norvaline oligopeptides by high resolution proton magnetic resonance
50. Nitrogen-15 magnetic resonance spectroscopy. Natural abundance spectra of isomeric homo-oligopeptides of L-norvaline and L-valine to the tetramers
51. Formation and stability of spiro-compounds. I. Spiro-compounds from cyclohexane